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- the base of the natural system of logarithms; approximately equal to 2.718282...
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2015/10/01 09:02:43」(JST)
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Eukaryotic translation elongation factor 2 |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
4V6X
|
|
|
Identifiers |
Symbols |
EEF2 ; EEF-2; EF-2; EF2; SCA26 |
External IDs |
OMIM: 130610 MGI: 95288 HomoloGene: 134867 ChEMBL: 1795108 GeneCards: EEF2 Gene |
Gene ontology |
Molecular function |
• translation elongation factor activity
• GTPase activity
• protein binding
• GTP binding
• protein kinase binding
• poly(A) RNA binding
|
Cellular component |
• nucleus
• cytoplasm
• cytosol
• polysome
• plasma membrane
• membrane
• aggresome
• ribonucleoprotein complex
• extracellular exosome
|
Biological process |
• hematopoietic progenitor cell differentiation
• translation
• translational elongation
• gene expression
• peptidyl-diphthamide biosynthetic process from peptidyl-histidine
• post-translational protein modification
• cellular protein metabolic process
• positive regulation of translation
|
Sources: Amigo / QuickGO |
|
RNA expression pattern |
|
|
More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
1938 |
13629 |
Ensembl |
ENSG00000167658 |
ENSMUSG00000034994 |
UniProt |
P13639 |
P58252 |
RefSeq (mRNA) |
NM_001961 |
NM_007907 |
RefSeq (protein) |
NP_001952 |
NP_031933 |
Location (UCSC) |
Chr 19:
3.98 – 3.99 Mb |
Chr 10:
81.18 – 81.18 Mb |
PubMed search |
[1] |
[2] |
|
Eukaryotic elongation factor 2 is a protein that in humans is encoded by the EEF2 gene.[1][2][3]
This gene encodes a member of the GTP-binding translation elongation factor family. This protein is an essential factor for protein synthesis. It promotes the GTP-dependent translocation of the ribosome. This protein is completely inactivated by EF-2 kinase phosphorylation.[3]
It is the target of diphtheria toxin and exotoxin A.[4]
References
- ^ Rapp G, Klaudiny J, Hagendorff G, Luck MR, Scheit KH (Mar 1990). "Complete sequence of the coding region of human elongation factor 2 (EF-2) by enzymatic amplification of cDNA from human ovarian granulosa cells". Biol Chem Hoppe Seyler 370 (10): 1071–5. doi:10.1515/bchm3.1989.370.2.1071. PMID 2610926.
- ^ Kaneda Y, Yoshida MC, Kohno K, Uchida T, Okada Y (Jul 1984). "Chromosomal assignment of the gene for human elongation factor 2". Proc Natl Acad Sci U S A 81 (10): 3158–62. doi:10.1073/pnas.81.10.3158. PMC 345240. PMID 6427766.
- ^ a b "Entrez Gene: EEF2 eukaryotic translation elongation factor 2".
- ^ Jørgensen R, Merrill AR, Andersen GR (February 2006). "The life and death of translation elongation factor 2". Biochem. Soc. Trans. 34 (Pt 1): 1–6. doi:10.1042/BST20060001. PMID 16246167.
Further reading
- Hanes J, Freudenstein J, Rapp G, Scheit KH (1992). "Construction of a plasmid containing the complete coding region of human elongation factor 2.". Biol. Chem. Hoppe-Seyler 373 (4): 201–4. doi:10.1515/bchm3.1992.373.1.201. PMID 1596361.
- Nygård O, Nilsson L (1990). "Kinetic determination of the effects of ADP-ribosylation on the interaction of eukaryotic elongation factor 2 with ribosomes.". J. Biol. Chem. 265 (11): 6030–4. PMID 2318846.
- Rapp G, Mucha J, Einspanier R; et al. (1988). "Cloning and sequence analysis of a cDNA from human ovarian granulosa cells encoding the C-terminal part of human elongation factor 2.". Biol. Chem. Hoppe-Seyler 369 (4): 247–50. doi:10.1515/bchm3.1988.369.1.247. PMID 2840927.
- Kaneda Y, Hayes H, Uchida T; et al. (1987). "Regional assignment of five genes on human chromosome 19.". Chromosoma 95 (1): 8–12. doi:10.1007/BF00293835. PMID 3034518.
- Nairn AC, Palfrey HC (1988). "Identification of the major Mr 100,000 substrate for calmodulin-dependent protein kinase III in mammalian cells as elongation factor-2.". J. Biol. Chem. 262 (36): 17299–303. PMID 3693353.
- Shestakova EA, Motuz LP, Minin AA, Gavrilova LP (1993). "Study of localization of the protein-synthesizing machinery along actin filament bundles.". Cell Biol. Int. 17 (4): 409–16. doi:10.1006/cbir.1993.1079. PMID 8318952.
- Redpath NT, Price NT, Severinov KV, Proud CG (1993). "Regulation of elongation factor-2 by multisite phosphorylation.". Eur. J. Biochem. 213 (2): 689–99. doi:10.1111/j.1432-1033.1993.tb17809.x. PMID 8386634.
- Knebel A, Haydon CE, Morrice N, Cohen P (2002). "Stress-induced regulation of eukaryotic elongation factor 2 kinase by SB 203580-sensitive and -insensitive pathways.". Biochem. J. 367 (Pt 2): 525–32. doi:10.1042/BJ20020916. PMC 1222910. PMID 12171600.
- Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Yin X, Fontoura BM, Morimoto T, Carroll RB (2003). "Cytoplasmic complex of p53 and eEF2.". J. Cell. Physiol. 196 (3): 474–82. doi:10.1002/jcp.10329. PMID 12891704.
- Ryazanova LV, Dorovkov MV, Ansari A, Ryazanov AG (2004). "Characterization of the protein kinase activity of TRPM7/ChaK1, a protein kinase fused to the transient receptor potential ion channel.". J. Biol. Chem. 279 (5): 3708–16. doi:10.1074/jbc.M308820200. PMID 14594813.
- Beausoleil SA, Jedrychowski M, Schwartz D; et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins.". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Gerhard DS, Wagner L, Feingold EA; et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Elo MA, Karjalainen HM, Sironen RK; et al. (2005). "High hydrostatic pressure inhibits the biosynthesis of eukaryotic elongation factor-2.". J. Cell. Biochem. 94 (3): 497–507. doi:10.1002/jcb.20333. PMID 15534876.
- Andersen JS, Lam YW, Leung AK; et al. (2005). "Nucleolar proteome dynamics.". Nature 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Shibatani T, David LL, McCormack AL; et al. (2005). "Proteomic analysis of mammalian oligosaccharyltransferase reveals multiple subcomplexes that contain Sec61, TRAP, and two potential new subunits.". Biochemistry 44 (16): 5982–92. doi:10.1021/bi047328f. PMID 15835887.
- Ahmed M, Forsberg J, Bergsten P (2005). "Protein profiling of human pancreatic islets by two-dimensional gel electrophoresis and mass spectrometry.". J. Proteome Res. 4 (3): 931–40. doi:10.1021/pr050024a. PMID 15952740.
- Gevaert K, Staes A, Van Damme J; et al. (2006). "Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC.". Proteomics 5 (14): 3589–99. doi:10.1002/pmic.200401217. PMID 16097034.
External links
- Peptide Elongation Factor 2 at the US National Library of Medicine Medical Subject Headings (MeSH)
English Journal
- Characterization of anti-P monoclonal antibodies directed against the ribosomal protein-RNA complex antigen and produced using Murphy Roths large autoimmune-prone mice.
- Sato H1, Onozuka M, Hagiya A, Hoshino S, Narita I, Uchiumi T.
- Clinical and experimental immunology.Clin Exp Immunol.2015 Feb;179(2):236-44. doi: 10.1111/cei.12460.
- Autoantibodies, including anti-ribosomal P proteins (anti-P), are thought to be produced by an antigen-driven immune response in systemic lupus erythematosus (SLE). To test this hypothesis, we reconstituted the ribosomal antigenic complex in vitro using human P0, phosphorylated P1 and P2 and a 28S r
- PMID 25255895
- eEF-2 Phosphorylation Down-Regulates P-Glycoprotein Over-Expression in Rat Brain Microvessel Endothelial Cells.
- Tang XH1, Wu XY1, Xu L1, Fang YX1, Wang P1, Zhu GX1, Hong Z1.
- PloS one.PLoS One.2015 May 11;10(5):e0125389. doi: 10.1371/journal.pone.0125389. eCollection 2015.
- OBJECTIVE: We investigated whether glutamate, NMDA receptors, and eukaryote elongation factor-2 kinase (eEF-2K)/eEF-2 regulate P-glycoprotein expression, and the effects of the eEF-2K inhibitor NH125 on the expression of P-glycoprotein in rat brain microvessel endothelial cells (RBMECs).METHODS: Cor
- PMID 25962137
- Reversible covalent inhibition of eEF-2K by carbonitriles.
- Devkota AK1, Edupuganti R, Yan C, Shi Y, Jose J, Wang Q, Kaoud TS, Cho EJ, Ren P, Dalby KN.
- Chembiochem : a European journal of chemical biology.Chembiochem.2014 Nov 3;15(16):2435-42. doi: 10.1002/cbic.201402321. Epub 2014 Sep 15.
- eEF-2K is a potential target for treating cancer. However, potent specific inhibitors for this enzyme are lacking. Previously, we identified 2,6-diamino-4-(2-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile (DFTD) as an inhibitor of eEF-2K. Here we describe its mechanism of action against eEF-2K, on th
- PMID 25224652
Japanese Journal
- 『カルモジュリンと高血圧症メカニズムの新展開』 高血圧症の病態を制御する新たなカルモジュリン関連タンパク質の血管系における機能
- 臼井 達哉,岡田 宗善,原 幸男 [他],山脇 英之
- 日本薬理学雑誌 141(2), 85-89, 2013
- … Ca2+結合タンパク質であるカルモジュリン(CaM)はCaM依存性(関連)タンパク質の機能調節を介して筋収縮,免疫応答,代謝,神経成長といった様々な細胞機能に影響を与える.最近,CaMおよびCaM依存性プロテインキナーゼ(CaMK)IIが心血管疾患の病態進展に関わるという報告がなされた.高血圧症の病態ではTNF-<I>α</I>やIL-6といった炎症性サイトカインの血中濃度が上昇し,活性酸素種(reactive oxygen …
- NAID 130003362534
- Comparative Study of the in Vitro Protective Effects of Several Antioxidants on Elongation Factor 2 under Oxidative Stress Conditions
- , , [他],
- Bioscience, biotechnology, and biochemistry 74(7), 1373-1379, 2010-07-23
- … Previous reports from our laboratory have indicated that the elongation step is specially affected by aging as a consequence of alterations in elongation factor-2 (eEF-2). … the effectiveness of several individual nutritional antioxidants in protecting the levels of hepatic eEF-2 subjected to oxidative stress induced by cumene hydroperoxide. …
- NAID 10027557055
- Trp^<221> is involved in the protective effect of elongation factor eEF-2 on te ricin/α-sarcin site of the ribosome
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★リンクテーブル★
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- 同
- eEF-2
- 同
- eEF-2